Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation.

When bacterial or eukaryotic cells are exposed to high temperatures or other harsh conditions, they respond by synthesis of a specific set of heat-shock proteins. Certain heat-shock proteins such as groEL, called 'chaperonins', can prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under harmful conditions. We report here a new aspect of the heat-shock response in Escherichia coli: at high temperatures a fraction of groEL becomes modified covalently, altering its interaction with unfolded proteins. The heat-modified form can be eluted with ATP from an unfolded protein more easily than normal groEL. The critical heat-induced modification seems to be phosphorylation, which is reversed on return to low temperature. Treatment of the modified groEL with phosphatases caused its apparent size, charge and binding properties to resemble those of the unmodified form. Thus during heat shock some groEL is reversibly phosphorylated, which allows its ATP-dependent release from protein substrates in the absence of its usual cofactor (groES), and probably promotes the repair of damaged polypeptides.     

Mate guarding as paternity insurance in Idaho ground squirrels

Following a copulation, males in many species of vertebrates (particularly birds) and invertebrates remain near the inseminated female and repel other suitors with displays or force. Guarding males must delay resumption of competitive mate searching, but they may insure their paternity by reducing possibilities for secondary matings and sperm competition. Among mammals, post-copulatory mate guarding has been reported in rodents, mongooses, ungulates and primates, including humans, but the effects of such behaviour on male reproductive success have not been determined genetically. I report here that mate guarding by male Idaho ground squirrels (Spermophilus brunneus) enhances a male's probability of paternity. Furthermore, an analysis based on game theory shows that mate guarding is an evolutionarily stable strategy for male S. brunneus, but not male Belding's ground squirrels (S. beldingi), which resume searching once copulation is completed.     

Peptide-dependent recognition of H-2Kb by alloreactive cytotoxic T lymphocytes

Antigen-specific T lymphocytes appear to recognize foreign antigens in the form of peptide fragments presented within the antigen-binding groove of class I or class II molecules encoded by the major histocompatibility complex (MHC). Alloreactive T cells also show specificity for MHC molecules, and various reports suggest that residues of the MHC molecules constitute at least part of the ligand to which alloreactive T-cell receptors bind. The X-ray crystal structure of the human MHC class I molecule, HLA-A2, has provided evidence to strengthen the argument that MHC-bound self-peptide might also contribute to such recognition. We now provide direct evidence for this, showing that at least some alloreactive cytotoxic T lymphocyte clones recognize peptide fragments derived from cytoplasmic proteins. We reasoned that if self-peptides were involved in allorecognition, then the sequence of some of these peptides could vary between species, resulting in species-restricted distribution of the relevant ligand(s). Several alloreactive cytotoxic T lymphocyte clones specific for H-2Kb, expressed by the murine cell line EL4, did not lyse a human-cell transfectant expressing the H-2Kb molecule (Jurkat-Kb cells). However, these clones were able to lyse Jurkat-Kb cells sensitized by preincubation with an EL4 cytoplasmic extract cleaved by cyanogen bromide. The sensitizing activity from this extract was destroyed by protease and appeared to be due to a peptide consisting of 10 to 15 amino acids.     

Genome evolution in yeasts

Identifying the mechanisms of eukaryotic genome evolution by comparative genomics is often complicated by the multiplicity of events that have taken place throughout the history of individual lineages, leaving only distorted and superimposed traces in the genome of each living organism. The hemiascomycete yeasts, with their compact genomes, similar lifestyle and distinct sexual and physiological properties, provide a unique opportunity to explore such mechanisms. We present here the complete, assembled genome sequences of four yeast species, selected to represent a broad evolutionary range within a single eukaryotic phylum, that after analysis proved to be molecularly as diverse as the entire phylum of chordates. A total of approximately 24,200 novel genes were identified, the translation products of which were classified together with Saccharomyces cerevisiae proteins into about 4,700 families, forming the basis for interspecific comparisons. Analysis of chromosome maps and genome redundancies reveal that the different yeast lineages have evolved through a marked interplay between several distinct molecular mechanisms, including tandem gene repeat formation, segmental duplication, a massive genome duplication and extensive gene loss.     

Fossiliferous Lana'i deposits formed by multiple events rather than a single giant tsunami

Giant tsunamis, generated by submarine landslides in the Hawaiian Islands, have been thought to be responsible for the deposition of chaotic gravels high on the southern coastal slopes of the islands of Lana'i and Moloka'i, Hawaii. Here we investigate this hypothesis, using uranium-thorium dating of the Hulopoe gravel (on Lana'i) and a study of stratigraphic relationships, such as facies changes and hiatuses, within the deposit. The Hulopoe gravel contains corals of two age groups, representing marine isotope stages 5e and 7 (approximately 135,000 and 240,000 years ago, respectively), with significant geographical and stratigraphic ordering. We show that the Hulopoe gravel was formed by multiple depositional events, separated by considerable periods of time, thus invalidating the main premise of the 'giant wave' hypothesis. Instead, the gravels were probably deposited during interglacial periods (when sea level was relatively high) by typical Hawaiian shoreline processes such as seasonal wave patterns, storm events and possibly 'normal' tsunamis, and reached their present height by uplift of Lana'i.     

Structure of the acrosomal bundle

In the unactivated Limulus sperm, a 60- micro m-long bundle of actin filaments crosslinked by the protein scruin is bent and twisted into a coil around the base of the nucleus. At fertilization, the bundle uncoils and fully extends in five seconds to support a finger of membrane known as the acrosomal process. This biological spring is powered by stored elastic energy and does not require the action of motor proteins or actin polymerization. In a 9.5-A electron cryomicroscopic structure of the extended bundle, we show that twist, tilt and rotation of actin-scruin subunits deviate widely from a 'standard' F-actin filament. This variability in structural organization allows filaments to pack into a highly ordered and rigid bundle in the extended state and suggests a mechanism for storing and releasing energy between coiled and extended states without disassembly.